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END3_CANAL
ID   END3_CANAL              Reviewed;         395 AA.
AC   Q5AJ82; A0A1D8PJ48;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE   AltName: Full=Endocytosis protein 3;
GN   Name=END3; OrderedLocusNames=CAALFM_C301400WA;
GN   ORFNames=CaO19.1711, CaO19.9278;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   INDUCTION.
RX   PubMed=15274137; DOI=10.1002/pmic.200300760;
RA   Yin Z., Stead D., Selway L., Walker J., Riba-Garcia I., McLnerney T.,
RA   Gaskell S., Oliver S.G., Cash P., Brown A.J.;
RT   "Proteomic response to amino acid starvation in Candida albicans and
RT   Saccharomyces cerevisiae.";
RL   Proteomics 4:2425-2436(2004).
CC   -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC       required for the internalization of endosomes during actin-coupled
CC       endocytosis. The complex links the site of endocytosis to the cell
CC       membrane-associated actin cytoskeleton. Mediates uptake of external
CC       molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC       role in the proper organization of the cell membrane-associated actin
CC       cytoskeleton and promotes its destabilization (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Regulated by GCN4 and induced in response to amino acid
CC       starvation. {ECO:0000269|PubMed:15274137}.
CC   -!- SIMILARITY: Belongs to the END3 family. {ECO:0000305}.
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DR   EMBL; CP017625; AOW28182.1; -; Genomic_DNA.
DR   RefSeq; XP_721782.1; XM_716689.1.
DR   AlphaFoldDB; Q5AJ82; -.
DR   STRING; 237561.Q5AJ82; -.
DR   GeneID; 3636644; -.
DR   KEGG; cal:CAALFM_C301400WA; -.
DR   CGD; CAL0000174035; END3.
DR   VEuPathDB; FungiDB:C3_01400W_A; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_040829_0_0_1; -.
DR   InParanoid; Q5AJ82; -.
DR   OMA; SNKIDYQ; -.
DR   OrthoDB; 597979at2759; -.
DR   PRO; PR:Q5AJ82; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   CDD; cd00052; EH; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR025604; End3.
DR   Pfam; PF12763; EF-hand_4; 1.
DR   Pfam; PF12761; End3; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM00027; EH; 2.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..395
FT                   /note="Actin cytoskeleton-regulatory complex protein END3"
FT                   /id="PRO_0000349443"
FT   DOMAIN          8..98
FT                   /note="EH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          40..75
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          136..225
FT                   /note="EH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   REGION          305..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          285..395
FT                   /evidence="ECO:0000255"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   395 AA;  44983 MW;  97584C909D9518D0 CRC64;
     MPRLEESEIK KYWQIFQSLK PQNNKLTGDQ LSSILKNSQL PQQQLSAIWE LSDIDNDGKL
     DFEEFCIIMR LIFDVINGKL PNVPQELPSW LIPASKSAII QANKAVNQGN NNFGDIDDDE
     DDKLSNDFDW YISPTDKSIY EKIYDSKCDS FGRIKYSSLN ELYNGLTNVP SSEISSAWNL
     INPKSFETID KDQTLVFLHI LNQRENGKRI PRGVPASLRA TFSKEVPNYD LSAQAKPSIS
     ATTETGKKSF AENYLNKIGG GVGASSTINN GRNEKGTDFS ATQGTDWEEV RLRRELQDLE
     RLLDKVQNDT KNQKDNSNNN QDNNDMLIKY EFEQLLKYKQ NQLNSTTNAS KNSTDLSSVK
     QDIEEIQNQV NTLQEFLTTK NQELLKLNQQ IESLK
 
 
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